Induced Fit Model
Induced Fit Model - Related Videos
01:58
Studying the Permeation of FITC and FITC-Ferritin through an In Vitro Blood-Brain Barrier Model
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2025
This video demonstrates a method to study permeation through an in vitro blood-brain barrier (BBB) model using astrocytes and endothelial cells on a membrane insert, with free FITC and FITC-loaded ferritin. FITC-ferritin bound to receptors on endothelial cells and crossed the membrane barrier to the lower chamber while free FITC showed restricted permeation and remained in the upper chamber.
02:56
FITC-Dextran Feeding: A Method to Quantify Intestinal Permeability in C. elegans
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2023
This video introduces a method of to visualize and measure the integrity of the C. elegans intestine lumen by feeding worms FITC-labeled dextran. The example protocol shows the assay done with 3,3’-diindolylmethane (DIM)-treated and pathogen-fed worms.
11:13
In Vitro Permeation of FITC-loaded Ferritins Across a Rat Blood-brain Barrier: a Model to Study the Delivery of Nanoformulated Molecules
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Cited by 15 •
2016
A method to establish an in vitro model of blood-brain barrier based on a co-culture of rat brain microvascular endothelial cells and astrocytes is described and validated. This system proved to be a valid tool to study the effect of nanoformulation on the trans-barrier permeation of fluorescent molecules.
01:13
Induced-fit Model
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2019
Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon. Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
04:50
Imaging FITC-dextran as a Reporter for Regulated Exocytosis
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Cited by 10 •
2018
Here we detail a method for live cell imaging of regulated exocytosis. This method utilizes FITC-dextran, which accumulates in lysosome-related organelles, as a reporter. This simple method also allows distinguishing between different modes of regulated exocytosis in cells that are difficult to manipulate genetically.
FAQs
The initial contact is not merely a final docking event; it is a reversible interaction that can promote movement of active-site residues. Those conformational adjustments may improve contacts with the substrate, arrange catalytic groups more effectively, and create a reaction environment better suited to the enzyme’s chemistry. This makes binding dynamically connected to catalysis.
Unlike a completely rigid lock-and-key picture, the induced fit model assigns functional importance to receptor flexibility. Complementarity develops through binding-related shape changes, rather than existing fully before the ligand arrives. This comparison helps explain why molecular recognition can accommodate precise interactions while still depending on conformational rearrangements within the protein or other receptor.
Transition-state stabilization is important because it links structural rearrangement to catalytic efficiency. When binding-induced changes position catalytic groups and improve active-site complementarity, the receptor can better support the high-energy transition state of the reaction. The model therefore connects molecular motion with the observed ability of an enzyme to accelerate a chemical transformation.
Changes in shape can influence both which ligands bind and how productively they are handled after binding. A substrate that promotes favorable contacts and catalytic-group positioning may show greater compatibility with the active site, helping account for enzyme specificity and catalytic efficiency. Thus, recognition is evaluated through its functional consequences, not binding alone.
Within chemistry, the model provides a way to interpret allosteric regulation as a consequence of biologically meaningful conformational flexibility. Changes in receptor shape are not treated as incidental movements; they can be part of how binding behavior and function are controlled. This perspective broadens molecular recognition beyond a single, permanently fixed active-site geometry.
Researchers can apply the model when interpreting kinetic data or planning structure-based drug design. Kinetic observations can be considered alongside changes in specificity and catalytic efficiency, while structural design can account for the receptor’s ability to adjust around a ligand. This approach encourages attention to adaptable binding interactions rather than assuming that one rigid shape determines recognition.